ID   TIM9_NEUCR              Reviewed;          88 AA.
AC   Q8J1Z1;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=Mitochondrial import inner membrane translocase subunit tim9;
GN   Name=tim9; ORFNames=NCU00198;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX   PubMed=14668492; DOI=10.1091/mbc.e03-05-0272;
RA   Vasiljev A., Ahting U., Nargang F.E., Go N.E., Habib S.J., Kozany C.,
RA   Panneels V., Sinning I., Prokisch H., Neupert W., Nussberger S.,
RA   Rapaport D.;
RT   "Reconstituted TOM core complex and Tim9/Tim10 complex of mitochondria are
RT   sufficient for translocation of the ADP/ATP carrier across membranes.";
RL   Mol. Biol. Cell 15:1445-1458(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
CC   -!- FUNCTION: Mitochondrial intermembrane chaperone that participates in
CC       the import and insertion of multi-pass transmembrane proteins into the
CC       mitochondrial inner membrane. Also required for the transfer of beta-
CC       barrel precursors from the TOM complex to the sorting and assembly
CC       machinery (SAM complex) of the outer membrane. Acts as a chaperone-like
CC       protein that protects the hydrophobic precursors from aggregation and
CC       guide them through the mitochondrial intermembrane space.
CC       {ECO:0000269|PubMed:14668492}.
CC   -!- SUBUNIT: Heterohexamer; composed of 3 copies of tim9 and 3 copies of
CC       tim10, named soluble 70 kDa complex. Associates with the tim22 complex,
CC       whose core is composed of tim22 and tim54. Interacts with the
CC       transmembrane regions of multi-pass transmembrane proteins in transit.
CC       {ECO:0000269|PubMed:14668492}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000269|PubMed:14668492}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:14668492}; Intermembrane side
CC       {ECO:0000269|PubMed:14668492}.
CC   -!- DOMAIN: The twin CX3C motif contains 4 conserved Cys residues that form
CC       2 disulfide bonds in the mitochondrial intermembrane space. However,
CC       during the transit of tim9 from cytoplasm into mitochondrion, the Cys
CC       residues probably coordinate zinc, thereby preventing folding and
CC       allowing its transfer across mitochondrial outer membrane (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the small Tim family. {ECO:0000305}.
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DR   EMBL; AY141127; AAN17751.1; -; mRNA.
DR   EMBL; CM002238; EAA27347.1; -; Genomic_DNA.
DR   RefSeq; XP_956583.1; XM_951490.2.
DR   AlphaFoldDB; Q8J1Z1; -.
DR   SMR; Q8J1Z1; -.
DR   STRING; 5141.EFNCRP00000000062; -.
DR   EnsemblFungi; EAA27347; EAA27347; NCU00198.
DR   GeneID; 3872730; -.
DR   KEGG; ncr:NCU00198; -.
DR   VEuPathDB; FungiDB:NCU00198; -.
DR   HOGENOM; CLU_141397_3_0_1; -.
DR   InParanoid; Q8J1Z1; -.
DR   Proteomes; UP000001805; Chromosome 3, Linkage Group III.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.287.810; -; 1.
DR   InterPro; IPR004217; Tim10-like.
DR   InterPro; IPR035427; Tim10-like_dom_sf.
DR   Pfam; PF02953; zf-Tim10_DDP; 1.
DR   SUPFAM; SSF144122; SSF144122; 1.
PE   1: Evidence at protein level;
KW   Chaperone; Disulfide bond; Membrane; Metal-binding; Mitochondrion;
KW   Mitochondrion inner membrane; Protein transport; Reference proteome;
KW   Translocation; Transport; Zinc.
FT   CHAIN           1..88
FT                   /note="Mitochondrial import inner membrane translocase
FT                   subunit tim9"
FT                   /id="PRO_0000228046"
FT   MOTIF           35..59
FT                   /note="Twin CX3C motif"
FT   DISULFID        35..59
FT                   /evidence="ECO:0000250"
FT   DISULFID        39..55
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   88 AA;  9860 MW;  B835637C0B01E711 CRC64;
     MDGLTAAESR ELDQRLQKRQ VKEFMSVFGN LVDNCFTACV DDFTSKALSG RESGCISRCV
     LKSMSTQTRL GERFGELNAA MTAEMQRR